Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 4.2.1.11 - phosphopyruvate hydratase and Organism(s) Escherichia coli and UniProt Accession P0A6P9

for references in articles please use BRENDA:EC4.2.1.11
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.11 phosphopyruvate hydratase
IUBMB Comments
Also acts on 3-phospho-D-erythronate.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Escherichia coli
UNIPROT: P0A6P9
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
neuron-specific enolase, enolase, neuron specific enolase, alpha-enolase, gamma-enolase, enolase 1, beta-enolase, yeast enolase, enolase 2, eno-1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-phospho-D-glycerate hydro-lyase
-
-
-
-
2-phosphoglycerate dehydratase
-
-
-
-
2-phosphoglycerate enolase
-
-
-
-
2-phosphoglyceric dehydratase
-
-
-
-
alpha,alpha-enolase
-
-
-
-
Alt a XI
-
-
-
-
beta,beta-enolase
-
-
-
-
Cla h VI
-
-
-
-
enolase
gamma,gamma-enolase
-
-
-
-
gamma-enolase
-
-
-
-
HLE1
-
-
-
-
hydratase, phosphoenolpyruvate
-
-
-
-
Laminin binding protein
-
-
-
-
Major allergen Alt a 11
-
-
-
-
MSE
-
-
-
-
Neural enolase
-
-
-
-
neuron-specific enolase
-
-
-
-
NNE
-
-
-
-
Non-neural enolase
-
-
-
-
NSE
-
-
-
-
OSE1
-
-
-
-
phosphoenolpyruvate hydratase
-
-
-
-
Phosphopyruvate hydratase
R-NSE
-
-
-
-
Skeletal muscle enolase
-
-
-
-
Tau-crystallin
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
-
-
-
-
addition
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
2-phospho-D-glycerate hydro-lyase (phosphoenolpyruvate-forming)
Also acts on 3-phospho-D-erythronate.
CAS REGISTRY NUMBER
COMMENTARY hide
9014-08-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
r
2-phospho-D-glycerate
phosphoenolpyruvate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-phospho-D-glycerate
phosphoenolpyruvate + H2O
show the reaction diagram
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
coordinated in catalytic site of enolase
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
260
-
pH 8.1, room temperature
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
as part of the degradosome complex
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45545
-
2 * 45545, mass spectrometry and X-ray crystallography
46000
-
2 * 46000, SDS-PAGE
90000
-
sedimentation velocity and sedimentation equilibrium experiments
92000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
1.6 A resolution, co-crystallization of enolase with a synthetic peptide corresponding to residues 833 to 850 from RNase E determined, asymmetric binding of a single molecule of RNase E to a conserved cleft at the interface of the enolase dimer
using the sitting drop method, co-crystallized with Mg2+
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using gel filtration chromatography
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Spring, T.G.; Wold, F.
The purification and characterization of Escherichia coli enolase
J. Biol. Chem.
246
6797-6802
1971
Escherichia coli
Manually annotated by BRENDA team
Spring, T.G.; Wold, F.
Enolase from Escherichia coli
Methods Enzymol.
42C
323-329
1975
Escherichia coli
-
Manually annotated by BRENDA team
Dannelly, H.K.; Reeves, H.C.
Purification and characterization of enolase from Escherichia coli
Curr. Microbiol.
17
265-268
1988
Escherichia coli
-
Manually annotated by BRENDA team
Kuhnel, K.; Luisi, B.F.
Crystal structure of the Escherichia coli RNA degradosome component enolase
J. Mol. Biol.
313
583-592
2001
Escherichia coli
Manually annotated by BRENDA team
Chandran, V.; Luisi, B.F.
Recognition of enolase in the Escherichia coli RNA degradosome
J. Mol. Biol.
358
8-15
2006
Escherichia coli (P0A6P9), Escherichia coli
Manually annotated by BRENDA team